Properties of the nucleotide binding sites of the Ca²⁺-ATPase of sarcoplasmic reticulum

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dc.contributor.advisorBerman, M Cen_ZA
dc.contributor.authorJeans, David Richarden_ZA
dc.date.accessioned2017-12-13T14:12:41Z
dc.date.available2017-12-13T14:12:41Z
dc.date.issued1988en_ZA
dc.description.abstractProperties of the nucleotide binding site of the Ca²⁺-ATPase of skeletal muscle sarcoplasmic reticulum have been investigated. The study centred around interaction of the high affinity ATP analog, 2'-3'-0-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate, (TNP-ATP), with the Ca²⁺-ATPase. Defined fractions of the sarcoplasmic reticulum (SR), corresponding to the terminal cisternae (TC) and light SR (LSR), were isolated. The TC were shown to have distinctive morphological characteristics that differ from the LSR. The TC vesicles contained electron dense intravesicular material representative of Ca²⁺ binding proteins, and visible membranous "feet" structures, which are reported to interconnect with the transverse tubule. Functional characterisation of the isolated fractions provided evidence for the predominant localisation of Ca²⁺ release channels in TC, and concentration of Ca²⁺-ATPase molecules in LSR. These conclusions were based on the following observations: (a) decreased Ca²⁺ transport of TC versus LSR; ruthenium red, a Ca²⁺ channel blocker, enhanced Ca²⁺ transport and pumping efficiency in TC, (b) higher Ca²⁺-ATPase activity for LSR in the presence and absence of ionophore, (c) rapid Ca²⁺ efflux from TC which is inhibited by ruthenium red. Of special interest was the characterisation of the TC and LSR with respect to turnover-dependent TNP-ATP fluorescence. Fluorescence observed for TC was approximately 65% of that for LSR. This phenomenon may be attributable to either the decreased Ca²⁺ ATPase content of the TC vesicles or open Ca²⁺ release channels. Hence the TNP-ATP fluorescence characteristics appear to reflect the morphological and functional subspecialisation of the defined SR fractions.en_ZA
dc.identifier.apacitationJeans, D. R. (1988). <i>Properties of the nucleotide binding sites of the Ca²⁺-ATPase of sarcoplasmic reticulum</i>. (Thesis). University of Cape Town ,Faculty of Health Sciences ,Division of Chemical Pathology. Retrieved from http://hdl.handle.net/11427/26592en_ZA
dc.identifier.chicagocitationJeans, David Richard. <i>"Properties of the nucleotide binding sites of the Ca²⁺-ATPase of sarcoplasmic reticulum."</i> Thesis., University of Cape Town ,Faculty of Health Sciences ,Division of Chemical Pathology, 1988. http://hdl.handle.net/11427/26592en_ZA
dc.identifier.citationJeans, D. 1988. Properties of the nucleotide binding sites of the Ca²⁺-ATPase of sarcoplasmic reticulum. University of Cape Town.en_ZA
dc.identifier.ris TY - Thesis / Dissertation AU - Jeans, David Richard AB - Properties of the nucleotide binding site of the Ca²⁺-ATPase of skeletal muscle sarcoplasmic reticulum have been investigated. The study centred around interaction of the high affinity ATP analog, 2'-3'-0-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate, (TNP-ATP), with the Ca²⁺-ATPase. Defined fractions of the sarcoplasmic reticulum (SR), corresponding to the terminal cisternae (TC) and light SR (LSR), were isolated. The TC were shown to have distinctive morphological characteristics that differ from the LSR. The TC vesicles contained electron dense intravesicular material representative of Ca²⁺ binding proteins, and visible membranous "feet" structures, which are reported to interconnect with the transverse tubule. Functional characterisation of the isolated fractions provided evidence for the predominant localisation of Ca²⁺ release channels in TC, and concentration of Ca²⁺-ATPase molecules in LSR. These conclusions were based on the following observations: (a) decreased Ca²⁺ transport of TC versus LSR; ruthenium red, a Ca²⁺ channel blocker, enhanced Ca²⁺ transport and pumping efficiency in TC, (b) higher Ca²⁺-ATPase activity for LSR in the presence and absence of ionophore, (c) rapid Ca²⁺ efflux from TC which is inhibited by ruthenium red. Of special interest was the characterisation of the TC and LSR with respect to turnover-dependent TNP-ATP fluorescence. Fluorescence observed for TC was approximately 65% of that for LSR. This phenomenon may be attributable to either the decreased Ca²⁺ ATPase content of the TC vesicles or open Ca²⁺ release channels. Hence the TNP-ATP fluorescence characteristics appear to reflect the morphological and functional subspecialisation of the defined SR fractions. DA - 1988 DB - OpenUCT DP - University of Cape Town LK - https://open.uct.ac.za PB - University of Cape Town PY - 1988 T1 - Properties of the nucleotide binding sites of the Ca²⁺-ATPase of sarcoplasmic reticulum TI - Properties of the nucleotide binding sites of the Ca²⁺-ATPase of sarcoplasmic reticulum UR - http://hdl.handle.net/11427/26592 ER - en_ZA
dc.identifier.urihttp://hdl.handle.net/11427/26592
dc.identifier.vancouvercitationJeans DR. Properties of the nucleotide binding sites of the Ca²⁺-ATPase of sarcoplasmic reticulum. [Thesis]. University of Cape Town ,Faculty of Health Sciences ,Division of Chemical Pathology, 1988 [cited yyyy month dd]. Available from: http://hdl.handle.net/11427/26592en_ZA
dc.language.isoengen_ZA
dc.publisher.departmentDivision of Chemical Pathologyen_ZA
dc.publisher.facultyFaculty of Health Sciencesen_ZA
dc.publisher.institutionUniversity of Cape Town
dc.subject.otherSarcoplasmic reticulum - Cytologyen_ZA
dc.subject.otherNucleotidesen_ZA
dc.subject.otherBinding sites (Biochemistry)en_ZA
dc.subject.otherAdenosine triphosphateen_ZA
dc.subject.otherCa²⁺-Transporting Atpaseen_ZA
dc.subject.otherBinding sitesen_ZA
dc.subject.otherNucleotidesen_ZA
dc.subject.otherSarcoplasmic Reticulum - physiologyen_ZA
dc.titleProperties of the nucleotide binding sites of the Ca²⁺-ATPase of sarcoplasmic reticulumen_ZA
dc.typeMaster Thesis
dc.type.qualificationlevelMasters
dc.type.qualificationnameMSc (Med)en_ZA
uct.type.filetypeText
uct.type.filetypeImage
uct.type.publicationResearchen_ZA
uct.type.resourceThesisen_ZA
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